ID A0A2G9HVU5_9LAMI Unreviewed; 960 AA.
AC A0A2G9HVU5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CDL12_05655 {ECO:0000313|EMBL:PIN21641.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN21641.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIN21641.1}.
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DR EMBL; NKXS01000910; PIN21641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9HVU5; -.
DR STRING; 429701.A0A2G9HVU5; -.
DR OrthoDB; 163787at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR48056:SF41; PROLINE IMINOPEPTIDASE; 1.
DR Pfam; PF00560; LRR_1; 6.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PIN21641.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:PIN21641.1};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIN21641.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..960
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013580662"
FT TRANSMEM 603..627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 663..956
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 691
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 960 AA; 106802 MW; 82FC2F080C96F27D CRC64;
MAVATIFRQV FHFLSFLCLL SITFSDELQT LLSIKTAFRD SNTRIFDSWE PNTPLCNFSG
ITCDSNGFVK EIELFNQNLT GLLPLSSFCQ LKSLESLSLG KNYLHGPVTE DLNKCFSLKY
LDLGINFFSG SFPDISSING LVYFLMDRSG FSGTFSWNSL RNMTNLQVLS LWDNPFDRTQ
FPTVILNLTK LNGLYLSNCS IEGNIPDEIG NLVELTELVL SENYLIGEIP RTITKLTKLC
ELELYFNELT GELPPGFGNL TSLEDFDASR NHLHGNLSEI RFLNKLKSLQ LFQNQFSGEV
PPELGDFKYL VDLSLYTNKL TGPLPQKLGS WADFIFIDVS ENFFTGPIPP DMCKKGTMVA
VLMLQNNFTG EIPDAYANCM TLIRFRVGKN RLSGQVPGGI WGLPKAELID VAKNDLEGPI
TSDIGKAKSL AQLLLAYNRL NGELPSEISK ASSLVSIDLS FNKFLGKIPE EIGELKQLTS
LQIQGNAFSG SIPDSLGSCH SINDVNMAKN MLSGSIPPSL GSLPALNFLN LSRNQLSGPI
PGTLSSLRLN LLDLSENRLT GQIPDSLLTE ANNSSFTGNL GLCNEKIRGF WQCSQQSGVS
GHLWMALFCL AFATIAMLAS LVAFCYLKKK RQNIGERSLK EDSWDLKPFH VLTFTMDEIL
DSIKQENLIG KGGSGNVYRV VVGNGKELAV KHIRYTDDRR KIGSSTCILN KRGTKCMEFE
AEVQTLSSIR HVNVVKLYCS ISGEDSNLLV YEYMPCGSLW DRLHSCNELE LDWETRYDIA
LGAAKGLEYL HHGCDGPVIH RDVKSSNILL DEELKPRIAD FGLAKIVQAN SMKESTQIIA
GTHGYIAPEY AYTNKVNEKS DLYSFGVVLM ELVTGKRPIE LEFGEDKNIV DWVSGNLKTK
ESVVRMVDPA IPEVYRESAI KVLKIAILCT ARLPTLRPTM RNVVQMVEEA QPRELVRVIE
//
